A0A0D2DUS1 · A0A0D2DUS1_9EURO

  • Protein
    Pentafunctional AROM polypeptide
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

function

The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site50-52NAD+ (UniProtKB | ChEBI)
Binding site87-90NAD+ (UniProtKB | ChEBI)
Binding site120-122NAD+ (UniProtKB | ChEBI)
Binding site125NAD+ (UniProtKB | ChEBI)
Binding site1367-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site145-146NAD+ (UniProtKB | ChEBI)
Binding site1527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1587-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site167NAD+ (UniProtKB | ChEBI)
Binding site1687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site185-188NAD+ (UniProtKB | ChEBI)
Binding site196NAD+ (UniProtKB | ChEBI)
Binding site200Zn2+ (UniProtKB | ChEBI); catalytic
Binding site200-2037-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site266Proton acceptor; for 3-dehydroquinate synthase activity
Binding site270-2747-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2777-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Active site281Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2937-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site293Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site829For EPSP synthase activity
Binding site877-884ATP (UniProtKB | ChEBI)
Active site1189Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1219Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-dehydroquinate dehydratase activity
Molecular Function3-dehydroquinate synthase activity
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionshikimate 3-dehydrogenase (NADP+) activity
Molecular Functionshikimate kinase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pentafunctional AROM polypeptide

Including 5 domains:

  • Recommended name
    3-dehydroquinate synthase
  • EC number
  • Short names
    DHQS
  • Recommended name
    3-phosphoshikimate 1-carboxyvinyltransferase
  • EC number
  • Alternative names
    • 5-enolpyruvylshikimate-3-phosphate synthase
      (EPSP synthase
      ; EPSPS
      )
  • Recommended name
    Shikimate kinase
  • EC number
  • Short names
    SK
  • Recommended name
    3-dehydroquinate dehydratase
  • EC number
  • Short names
    3-dehydroquinase
  • Recommended name
    Shikimate dehydrogenase
  • EC number

Gene names

    • ORF names
      PV04_08080

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 27337
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Phialophora

Accessions

  • Primary accession
    A0A0D2DUS1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3903-dehydroquinate synthase
Domain82-3643-dehydroquinate synthase
Domain415-841Enolpyruvate transferase
Region870-1062Shikimate kinase
Region1302-1619Shikimate dehydrogenase
Domain1307-1387Shikimate dehydrogenase substrate binding N-terminal

Sequence similarities

Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the dehydroquinate synthase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,619
  • Mass (Da)
    175,173
  • Last updated
    2015-04-29 v1
  • Checksum
    228FC4369F29CA83
MPLVNGTPKEVRVSLLGKESIIINFGLWRNDVASDLLTNLESSTYVLITDTTLGSLYVSAFQQAFTAASQRRSSPSRLLVHQIPPGESSKSRQTKDDIEDWLLSQSPPCGRDTVIIALGGGVVGDLTGFVAATYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAIWQPQRIYIDLEFLGTLPRRELINGMAEVIKTAAISDEEEFIALERNAERIMAAVNADISQGASRFKDIETILLRIISASASFKAHVVTIDERETGLRNLLNFGHSIGHAMEAFLTPQVLHGECVAIGMVKEAELSRYLGILSGVAVGRLQKCLTVYGLPTRLDDEKVRKLSGGKVCTVDGMLKKMGVDKKNDGAKKKVVLLSAIGRTYEQMASVVSDSDLRVVLSPSVEVIPGVPRDLSVVCIPPGSKSISNRALVLAALGQGTCRIKNLLTSADTEVMLQALTRLGAATFSWEEDGEVLVVNGNGGRLEATQHALYLGNAGTAARFLTSVATLTRQSHVASTVLTGNARMKQRPIGDLVDALRGNGAGIEYMESNGSLPLNITASAGFNGGEIKLAAKVSSQYVSSLLMCAPYAKKPVTLKLVGGKPVSQPYIDMTIAMMASFGVQVQKSKTEEHTYLIPQGTYRNPAEYIVESDASSATYPLAIAAMTGTTCTIPNIGSASLQGDSAFATDVLRPMGCEVKQTASSTTVTGPRNGKLLPLPNIDMEPMTDAFLTASVLAAVAQGSESNTTRIYGIANQRVKECNRIQAMEDELAKFGVTCRQFDDGIEIDGIDRSQLQQPQGGVHCYDDHRVAMSFSVLALAAPRPTLILEKECTGKTWPGWWDTMARQFSVKLQGVELEATNTSSRAKQLDRSAASIFIIGMRGAGKTTSGRWAARSLGKKLIDLDTELEIRERKTIPEVVREHGWDHFRQVELKLLKSVMEEMPNGYIFACGGGVVETAEARQLLVDWHQKKGHVLLVERNIAEVMDFLQIDKTRPAYVEDMMGVWLRRKPWFEQCSNILYYSQSIPNEQMSEAAEDFDRFLQFVTGKIDVLSKVKQKSESFFVALTFPDLRPHLSILPEVCLGSDAVELRVDLLKDPNSQTDVPSADYVTSQLSLLRATVPLPVVFTIRTLAQGGKFPNEAHAEYLNLCTLAMRMGAEFVDVEVASLPEDILTKLLAFKNNSYSKIIASHHDPRGTLSWSRPGSWIPIYNKCVQHGADIIKLIGVAGSLDDNFALRRFKQWSHAQHPELPLIAINMGTTGQISRILNGFMTPVSHPSLPFKAAPGQLSAQEIRRGLALIGSIPRKEFYLFGSPISASKSPALHNTLFEHTGLPHVYQLCETTDLEVIKTTIRSDDFGGASVTIPLKLDIMPLLDDVDASARLIGAVNTIVPTFDRVSGKNRLVGYNTDFLGMMDCLRGAGASAALGDGDQSGLVIGGGGTARAAIHTLHSMGYKPIYLVGRNHAKMVELARSFPPIYDLIVLDATLGPDGVVDAMMSARPNSPALPMVAIATVPANIPLDPVLGAALKAVFAHSKRIGATGSTAPKGQGSSPPARTLLELAYKPAHTAVMQMAEQLGGWKTVQGLETLVTQGLWQFEFWTGIRARDLGGRISRDVVLGPGA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN846960
EMBL· GenBank· DDBJ
KIW65862.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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